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CIPKX_ORYSJ
ID   CIPKX_ORYSJ             Reviewed;         454 AA.
AC   Q2RAX3; Q0IUU5;
DT   10-JUN-2008, integrated into UniProtKB/Swiss-Prot.
DT   24-JAN-2006, sequence version 1.
DT   03-AUG-2022, entry version 99.
DE   RecName: Full=CBL-interacting protein kinase 33;
DE            EC=2.7.11.1;
DE   AltName: Full=OsCIPK33;
GN   Name=CIPK33; OrderedLocusNames=Os11g0134300, LOC_Os11g03970;
OS   Oryza sativa subsp. japonica (Rice).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; Liliopsida; Poales; Poaceae; BOP clade;
OC   Oryzoideae; Oryzeae; Oryzinae; Oryza; Oryza sativa.
OX   NCBI_TaxID=39947;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. Nipponbare;
RX   PubMed=16188032; DOI=10.1186/1741-7007-3-20;
RG   The rice chromosomes 11 and 12 sequencing consortia;
RT   "The sequence of rice chromosomes 11 and 12, rich in disease resistance
RT   genes and recent gene duplications.";
RL   BMC Biol. 3:20-20(2005).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. Nipponbare;
RX   PubMed=16100779; DOI=10.1038/nature03895;
RG   International rice genome sequencing project (IRGSP);
RT   "The map-based sequence of the rice genome.";
RL   Nature 436:793-800(2005).
RN   [3]
RP   GENOME REANNOTATION.
RC   STRAIN=cv. Nipponbare;
RX   PubMed=18089549; DOI=10.1093/nar/gkm978;
RG   The rice annotation project (RAP);
RT   "The rice annotation project database (RAP-DB): 2008 update.";
RL   Nucleic Acids Res. 36:D1028-D1033(2008).
RN   [4]
RP   GENOME REANNOTATION.
RC   STRAIN=cv. Nipponbare;
RX   PubMed=24280374; DOI=10.1186/1939-8433-6-4;
RA   Kawahara Y., de la Bastide M., Hamilton J.P., Kanamori H., McCombie W.R.,
RA   Ouyang S., Schwartz D.C., Tanaka T., Wu J., Zhou S., Childs K.L.,
RA   Davidson R.M., Lin H., Quesada-Ocampo L., Vaillancourt B., Sakai H.,
RA   Lee S.S., Kim J., Numa H., Itoh T., Buell C.R., Matsumoto T.;
RT   "Improvement of the Oryza sativa Nipponbare reference genome using next
RT   generation sequence and optical map data.";
RL   Rice 6:4-4(2013).
RN   [5]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 50-454.
RC   STRAIN=cv. Nipponbare;
RX   PubMed=12869764; DOI=10.1126/science.1081288;
RG   The rice full-length cDNA consortium;
RT   "Collection, mapping, and annotation of over 28,000 cDNA clones from
RT   japonica rice.";
RL   Science 301:376-379(2003).
RN   [6]
RP   GENE FAMILY, AND NOMENCLATURE.
RX   PubMed=14730064; DOI=10.1104/pp.103.033068;
RA   Kolukisaoglu U., Weinl S., Blazevic D., Batistic O., Kudla J.;
RT   "Calcium sensors and their interacting protein kinases: genomics of the
RT   Arabidopsis and rice CBL-CIPK signaling networks.";
RL   Plant Physiol. 134:43-58(2004).
CC   -!- FUNCTION: CIPK serine-threonine protein kinases interact with CBL
CC       proteins. Binding of a CBL protein to the regulatory NAF domain of CIPK
CC       protein lead to the activation of the kinase in a calcium-dependent
CC       manner (By similarity). {ECO:0000250}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=ATP + L-seryl-[protein] = ADP + H(+) + O-phospho-L-seryl-
CC         [protein]; Xref=Rhea:RHEA:17989, Rhea:RHEA-COMP:9863, Rhea:RHEA-
CC         COMP:11604, ChEBI:CHEBI:15378, ChEBI:CHEBI:29999, ChEBI:CHEBI:30616,
CC         ChEBI:CHEBI:83421, ChEBI:CHEBI:456216; EC=2.7.11.1;
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=ATP + L-threonyl-[protein] = ADP + H(+) + O-phospho-L-
CC         threonyl-[protein]; Xref=Rhea:RHEA:46608, Rhea:RHEA-COMP:11060,
CC         Rhea:RHEA-COMP:11605, ChEBI:CHEBI:15378, ChEBI:CHEBI:30013,
CC         ChEBI:CHEBI:30616, ChEBI:CHEBI:61977, ChEBI:CHEBI:456216;
CC         EC=2.7.11.1;
CC   -!- COFACTOR:
CC       Name=Mn(2+); Xref=ChEBI:CHEBI:29035; Evidence={ECO:0000250};
CC   -!- DOMAIN: The activation loop within the kinase domain is the target of
CC       phosphorylation/activation by upstream protein kinases. The PPI motif
CC       mediates the interaction with the ABI (abscisic acid-insensitive)
CC       phosphatases (By similarity). {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the protein kinase superfamily. CAMK Ser/Thr
CC       protein kinase family. SNF1 subfamily. {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=BAF27520.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR   EMBL; DP000010; ABA91407.1; -; Genomic_DNA.
DR   EMBL; AP008217; BAF27520.1; ALT_INIT; Genomic_DNA.
DR   EMBL; AP014967; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AK112043; -; NOT_ANNOTATED_CDS; mRNA.
DR   RefSeq; XP_015617151.1; XM_015761665.1.
DR   RefSeq; XP_015617152.1; XM_015761666.1.
DR   AlphaFoldDB; Q2RAX3; -.
DR   SMR; Q2RAX3; -.
DR   STRING; 4530.OS11T0134300-01; -.
DR   PaxDb; Q2RAX3; -.
DR   PRIDE; Q2RAX3; -.
DR   GeneID; 4349698; -.
DR   KEGG; osa:4349698; -.
DR   eggNOG; KOG0583; Eukaryota.
DR   HOGENOM; CLU_000288_59_0_1; -.
DR   InParanoid; Q2RAX3; -.
DR   OrthoDB; 1127668at2759; -.
DR   Proteomes; UP000000763; Chromosome 11.
DR   Proteomes; UP000059680; Chromosome 11.
DR   Genevisible; Q2RAX3; OS.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0106310; F:protein serine kinase activity; IEA:RHEA.
DR   GO; GO:0004674; F:protein serine/threonine kinase activity; IBA:GO_Central.
DR   GO; GO:0035556; P:intracellular signal transduction; IBA:GO_Central.
DR   GO; GO:0006468; P:protein phosphorylation; IBA:GO_Central.
DR   InterPro; IPR011009; Kinase-like_dom_sf.
DR   InterPro; IPR018451; NAF/FISL_domain.
DR   InterPro; IPR004041; NAF_dom.
DR   InterPro; IPR000719; Prot_kinase_dom.
DR   InterPro; IPR017441; Protein_kinase_ATP_BS.
DR   InterPro; IPR008271; Ser/Thr_kinase_AS.
DR   Pfam; PF03822; NAF; 1.
DR   Pfam; PF00069; Pkinase; 1.
DR   SMART; SM00220; S_TKc; 1.
DR   SUPFAM; SSF56112; SSF56112; 1.
DR   PROSITE; PS50816; NAF; 1.
DR   PROSITE; PS00107; PROTEIN_KINASE_ATP; 1.
DR   PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
DR   PROSITE; PS00108; PROTEIN_KINASE_ST; 1.
PE   2: Evidence at transcript level;
KW   ATP-binding; Kinase; Manganese; Nucleotide-binding; Reference proteome;
KW   Serine/threonine-protein kinase; Transferase.
FT   CHAIN           1..454
FT                   /note="CBL-interacting protein kinase 33"
FT                   /id="PRO_0000338390"
FT   DOMAIN          13..268
FT                   /note="Protein kinase"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT   DOMAIN          305..329
FT                   /note="NAF"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00256"
FT   REGION          154..183
FT                   /note="Activation loop"
FT                   /evidence="ECO:0000250"
FT   REGION          335..364
FT                   /note="PPI"
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        136
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00159,
FT                   ECO:0000255|PROSITE-ProRule:PRU10027"
FT   BINDING         19..27
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT   BINDING         42
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
SQ   SEQUENCE   454 AA;  52056 MW;  2F205039FB21ADF2 CRC64;
     MSTTKVKRRV GKYELGRTIG EGTFAKVKFA RDTETGDPVA IKILDKEKVL KHKMVEQIKR
     EISTMKLIKH PNVVRIYEVM GSKTNIYIVL EYVTGGELFD TIVNHGRMRE DEARRYFQQL
     INAVDYCHSR GVYHRDLKPE NLLLDSYGNL KVSDFGLSAL SQQIKDDGLL HTTCGTPNYV
     APEVLEDQGY DGAMADLWSC GVILFVLLAG YLPFEDSNLM TLYKKISNAE FTFPPWTSFP
     AKRLLTRILD PNPMTRITIP EILEDEWFKK GYKRPEFDEK YDTTLDDVDA VFNDSEEHHV
     TEKKEEPEAL NAFELISMSA GLNLGNLFDS EQEFKRETRF TSKCPPKEIV RKIEEAAKPL
     GFDVQKKNYK ICSPCLTTIC MNIPFKLRLE KVKAGRKGNL NVATEILQVA PSLHMVEVRK
     AKGDTLEFHK FYKNLSRTLK DVVWKSDDLQ NQLS
 
 
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